Strongly correlated structure of axial‐symmetric proteins. III. Complexes with DNA/RNA
Identifieur interne : 002F89 ( Main/Merge ); précédent : 002F88; suivant : 002F90Strongly correlated structure of axial‐symmetric proteins. III. Complexes with DNA/RNA
Auteurs : A. Janner [Pays-Bas]Source :
- Acta Crystallographica Section D [ 1399-0047 ] ; 2005-03.
English descriptors
- Teeft :
- Acta, Acta cryst, Approximate symmetry, Asymmetric unit, Atom positions, Atomic positions, Attenuation protein, Axial, Axial ratio, Bacteriophage, Binding protein, Binding sites, Capsid, Central axis, Central hole, Centre, Coat protein, Conformation, Correlated structure, Cryst, Curvature cylinder, Double helix, Empty circles, Extremal distance, Form lattice, Free state, Helical, Helix, Histone, Histone octamer, Histone protein, Isometric, Janner, Janner proteins, Lamentous bacteriophage, Large number, Lateral boundaries, Lattice, Line segment, Major coat protein, Molecular form, Molecular form lattice, Nucleic acid, Nucleic acids, Nucleosome core particle, Nucleotide, Other parameters, Parameter, Polygon, Polygrammal, Protein, Protein subunit, Pyrococcus abyssi, Radius, Research papers, Same pitch, Shadow symmetry, Similar analysis, Similar architecture, Single parameter, Single strand, Star polygon, Star polygons, Structural correlations, Structural parameters, Subsystem, Subunit, Subunit height, Superhelical structure, Superhelix, Symmetry, Third situation, Total height, Trap envelope, Trap subsystem, Unit parameter, Unit rise.
Abstract
Three cases are considered of protein–DNA (or protein–RNA) complexes with a strongly correlated structure based on symmetry. In the first the symmetry of the nucleic acid is the determinant element, the second contains a dominant protein and an adaptive DNA/RNA and in the third a perturbed symmetry arises from elements of both components. The first situation is exemplified by the filamentous bacteriophage Pf1 in a low‐ and high‐temperature state. The Pyrococcus abyssi Sm core and the trp RNA‐binding attenuation protein are examples of the second situation. Finally, the nucleosome core particle represents the cooperative compromise between histone and DNA. In all the cases, the strong correlation in the structure is based on polygrammal scaling relations and on a molecular polygonal form lattice which depends on a single parameter.
Url:
DOI: 10.1107/S0907444904032718
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<pubPlace>5 Abbey Square, Chester, Cheshire CH1 2HU, England</pubPlace>
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<profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acta</term>
<term>Acta cryst</term>
<term>Approximate symmetry</term>
<term>Asymmetric unit</term>
<term>Atom positions</term>
<term>Atomic positions</term>
<term>Attenuation protein</term>
<term>Axial</term>
<term>Axial ratio</term>
<term>Bacteriophage</term>
<term>Binding protein</term>
<term>Binding sites</term>
<term>Capsid</term>
<term>Central axis</term>
<term>Central hole</term>
<term>Centre</term>
<term>Coat protein</term>
<term>Conformation</term>
<term>Correlated structure</term>
<term>Cryst</term>
<term>Curvature cylinder</term>
<term>Double helix</term>
<term>Empty circles</term>
<term>Extremal distance</term>
<term>Form lattice</term>
<term>Free state</term>
<term>Helical</term>
<term>Helix</term>
<term>Histone</term>
<term>Histone octamer</term>
<term>Histone protein</term>
<term>Isometric</term>
<term>Janner</term>
<term>Janner proteins</term>
<term>Lamentous bacteriophage</term>
<term>Large number</term>
<term>Lateral boundaries</term>
<term>Lattice</term>
<term>Line segment</term>
<term>Major coat protein</term>
<term>Molecular form</term>
<term>Molecular form lattice</term>
<term>Nucleic acid</term>
<term>Nucleic acids</term>
<term>Nucleosome core particle</term>
<term>Nucleotide</term>
<term>Other parameters</term>
<term>Parameter</term>
<term>Polygon</term>
<term>Polygrammal</term>
<term>Protein</term>
<term>Protein subunit</term>
<term>Pyrococcus abyssi</term>
<term>Radius</term>
<term>Research papers</term>
<term>Same pitch</term>
<term>Shadow symmetry</term>
<term>Similar analysis</term>
<term>Similar architecture</term>
<term>Single parameter</term>
<term>Single strand</term>
<term>Star polygon</term>
<term>Star polygons</term>
<term>Structural correlations</term>
<term>Structural parameters</term>
<term>Subsystem</term>
<term>Subunit</term>
<term>Subunit height</term>
<term>Superhelical structure</term>
<term>Superhelix</term>
<term>Symmetry</term>
<term>Third situation</term>
<term>Total height</term>
<term>Trap envelope</term>
<term>Trap subsystem</term>
<term>Unit parameter</term>
<term>Unit rise</term>
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<front><div type="abstract" xml:lang="en">Three cases are considered of protein–DNA (or protein–RNA) complexes with a strongly correlated structure based on symmetry. In the first the symmetry of the nucleic acid is the determinant element, the second contains a dominant protein and an adaptive DNA/RNA and in the third a perturbed symmetry arises from elements of both components. The first situation is exemplified by the filamentous bacteriophage Pf1 in a low‐ and high‐temperature state. The Pyrococcus abyssi Sm core and the trp RNA‐binding attenuation protein are examples of the second situation. Finally, the nucleosome core particle represents the cooperative compromise between histone and DNA. In all the cases, the strong correlation in the structure is based on polygrammal scaling relations and on a molecular polygonal form lattice which depends on a single parameter.</div>
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